Geometry of proteins: Hydrogen bonding, sterics, and marginally compact tubes

被引:13
作者
Banavar, JR [1 ]
Cieplak, M
Flammini, A
Hoang, TX
Kamien, RD
Lezon, T
Marenduzzo, D
Maritan, A
Seno, F
Snir, Y
Trovato, A
机构
[1] Penn State Univ, Dept Phys, Davey Lab 104, University Pk, PA 16802 USA
[2] Polish Acad Sci, Inst Phys, PL-02668 Warsaw, Poland
[3] Indiana Univ, Sch Informat, Bloomington, IN 47408 USA
[4] VAST, Inst Phys & Elect, Hanoi, Vietnam
[5] Univ Penn, Dept Phys & Astron, Philadelphia, PA 19104 USA
[6] Univ Warwick, Inst Math, Coventry CV4 7AL, W Midlands, England
[7] Univ Padua, Dipartimento Fis G Galilei, I-35131 Padua, Italy
[8] Univ Padua, Sez INFN, I-35131 Padua, Italy
来源
PHYSICAL REVIEW E | 2006年 / 73卷 / 03期
基金
美国国家科学基金会;
关键词
D O I
10.1103/PhysRevE.73.031921
中图分类号
O35 [流体力学]; O53 [等离子体物理学];
学科分类号
070204 ; 080103 ; 080704 ;
摘要
The functionality of proteins is governed by their structure in the native state. Protein structures are made up of emergent building blocks of helices and almost planar sheets. A simple coarse-grained geometrical model of a flexible tube barely subject to compaction provides a unified framework for understanding the common character of globular proteins. We argue that a recent critique of the tube idea is not well founded.
引用
收藏
页数:5
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